ID   ALD1_ACISP              Reviewed;         503 AA.
AC   Q9FDS1;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Long-chain-aldehyde dehydrogenase;
DE            EC=1.2.1.48;
DE   AltName: Full=Aldehyde dehydrogenase 1;
GN   Name=ald1;
OS   Acinetobacter sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-32 AND 480-489,
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP   ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M-1;
RX   PubMed=10919810; DOI=10.1128/aem.66.8.3481-3486.2000;
RA   Ishige T., Tani A., Sakai Y., Kato N.;
RT   "Long-chain aldehyde dehydrogenase that participates in n-alkane
RT   utilization and wax ester synthesis in Acinetobacter sp. strain M-1.";
RL   Appl. Environ. Microbiol. 66:3481-3486(2000).
CC   -!- FUNCTION: Aldehyde dehydrogenase that shows activity toward n-alkanals
CC       (C(4) to C(14)), with a preference for longer carbon chains. The best
CC       substrate is tetradecanal. {ECO:0000269|PubMed:10919810}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty aldehyde + H2O + NAD(+) = a long-chain
CC         fatty acid + 2 H(+) + NADH; Xref=Rhea:RHEA:10652, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17176, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57560, ChEBI:CHEBI:57945; EC=1.2.1.48;
CC         Evidence={ECO:0000269|PubMed:10919810};
CC   -!- ACTIVITY REGULATION: Completely inhibited by p-chloromercuribenzoate
CC       and N-ethylmaleimide. Strongly inhibited by iodoacetate. Inhibited by
CC       Pb(2+), Fe(3+), Ag(+) and Hg(2+) and partially inhibited by several
CC       other metal ions Mn(2+), Zn(2+) and Cu(2+).
CC       {ECO:0000269|PubMed:10919810}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.5. {ECO:0000269|PubMed:10919810};
CC       Temperature dependence:
CC         Optimum temperature is 43 degrees Celsius.
CC         {ECO:0000269|PubMed:10919810};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10919810}.
CC   -!- DISRUPTION PHENOTYPE: Reduced aldehyde dehydrogenase activity toward n-
CC       tetradecanal, although cells are still able to grow on n-hexadecane to
CC       some extent. {ECO:0000269|PubMed:10919810}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB042203; BAB11888.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9FDS1; -.
DR   SMR; Q9FDS1; -.
DR   GO; GO:0050061; F:long-chain-aldehyde dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..503
FT                   /note="Long-chain-aldehyde dehydrogenase"
FT                   /id="PRO_0000430454"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000250"
FT   BINDING         218..224
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   503 AA;  55499 MW;  3254DBACCC65F246 CRC64;
     MHYVDPNQSG SKIHFKDQYE NFIGGQWVAP VKGVYFDNIS PVDGKSFTRI PRSSAEDIEL
     ALDAAHKAKK EWNKSSPTTR SNLLLKIADR MEANLEMLAV AETWDNGKPV RETLAADIPL
     AIDHFRYFAG CIRAQEGGIS EIDEDTIAYH FHEPLGVVGQ IIPWNFPILM AAWKLAPALA
     AGNCVVIKPA EQTPVGILLV AELIQDLLPA GVLNIVNGYG AEVGRPLATS PRIAKIAFTG
     STQVGQLIMQ YATENIIPVT LELGGKSPNV FFADVMDHDD DFLDKTLEGF AMFALNQGEV
     CTCPSRALIQ ESIADQFMEK AIERVKRIKL GHPLDTDTMV GAQASLEQQE KILRCIDTGR
     QEGAEVLLGG HGRQEVGNGY YIEPTIFKGH NNMQVFQEEI FGPVLSVTTF KDFDEAIQIA
     NDTMYGLGAG VWSRSTHTAY RAGRAIEAGR VWTNCYHIYP AHAAFGGYKK SGVGRENHKM
     MLDHYQQTKN LLVSYSTKAM GFF